Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin

J Biol Chem. 1984 Jan 25;259(2):696-8.

Abstract

Transducin was [32P]ADP-ribosylated by cholera toxin in bovine retinal rod outer segments and then partially purified on omega-amino octyl agarose to remove other ADP-ribosylated proteins. Trypsin digestion of the ADP-ribosylated transducin and further purification using boronate-polyacrylamide beads and high performance liquid chromatography yielded a single radiolabeled tetrapeptide, Ser-Arg-Val-Lys. The ADP-ribose is linked to the guanidinium group of arginine.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Cholera Toxin / pharmacology*
  • Chromatography, High Pressure Liquid
  • Membrane Proteins / analysis*
  • Membrane Proteins / metabolism
  • Nucleoside Diphosphate Sugars / metabolism*
  • Photoreceptor Cells / analysis*
  • Rod Cell Outer Segment / analysis*
  • Transducin
  • Trypsin / metabolism

Substances

  • Membrane Proteins
  • Nucleoside Diphosphate Sugars
  • Adenosine Diphosphate Ribose
  • Cholera Toxin
  • Trypsin
  • Transducin